GM CSF Human, Pichia
Granulocyte Macrophage-Colony Stimulating Factor Human Recombinant, Pichia
Cat. No.
BT730
Source
Pichia Pastoris.
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 97.0% as determined by1. Analysis by RP-HPLC.
2. Analysis by SDS-PAGE.
2. Analysis by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description
Granulocyte Macrophage Colony Stimulating Factor Human Recombinant produced in Yeast is a single, glycosylated, polypeptide chain containing 127 amino acids and having a molecular mass of 26-32 kDa. rhGMCSF differs from the natural human GM-CSF by a substitution of leucine at position 23 (R to L), and the carbohydrate moiety may be different from the native protein.
GM-CSF is purified by proprietary chromatographic techniques.
GM-CSF is purified by proprietary chromatographic techniques.
Product Specs
Introduction
Granulocyte-macrophage colony-stimulating factor (GM-CSF) is a cytokine that plays a crucial role in the production, differentiation, and function of granulocytes and macrophages, which are essential components of the immune system. The active form of GM-CSF exists as a homodimer in the extracellular space. This gene encoding GM-CSF is located within a cluster of related genes on chromosome 5q31, a region associated with interstitial deletions observed in 5q- syndrome and acute myelogenous leukemia. Notably, this gene cluster also includes genes encoding interleukins 4, 5, and 13.
Description
Recombinant Human Granulocyte-Macrophage Colony-Stimulating Factor (rhGM-CSF), produced in Yeast, is a single, glycosylated polypeptide chain comprising 127 amino acids. With a molecular mass ranging from 26 to 32 kDa, rhGM-CSF differs slightly from its naturally occurring human counterpart. Specifically, it features a substitution of leucine for arginine at position 23 (R to L), and the composition of its carbohydrate moiety may vary from the native protein. The purification process of rhGM-CSF involves proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation
The protein was lyophilized from a concentrated solution (1 mg/ml) containing 10 mM phosphate buffer at pH 7.0, 40 mg/ml mannitol, and 10 mg/ml sucrose.
Solubility
For reconstitution of lyophilized Granulocyte Macrophage Colony Stimulating Factor, it is recommended to use sterile 18 MΩ-cm H2O. The initial reconstitution should be at a concentration not less than 100 µg/ml. This solution can then be further diluted to desired concentrations using other suitable aqueous solutions.
Stability
Lyophilized Granulocyte Macrophage Colony Stimulating Factor exhibits stability at room temperature for up to 3 weeks. However, for extended storage, it is recommended to store the lyophilized product desiccated at a temperature below -18°C. Upon reconstitution, GM-CSF should be stored at 4°C for a period of 2-7 days. For long-term storage of the reconstituted protein, it is advisable to add a carrier protein (0.1% HSA or BSA) and store below -18°C. Repeated freeze-thaw cycles should be avoided.
Purity
The purity of this product is determined using two methods: 1. Analysis by RP-HPLC and 2. Analysis by SDS-PAGE. The purity is greater than 97.0% as determined by both methods.
Biological Activity
The biological activity is determined by the dose-dependent stimulation of the proliferation of human TF-1 cells (a human erythroleukemic indicator cell line). This product has an ED50 of less than 0.183 ng/ml, corresponding to a Specific Activity of 5,500,000 IU/mg.
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.
Source
Pichia Pastoris.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.
Product Science Overview
Recombinant Production
Recombinant human GM-CSF (rhGM-CSF) is produced industrially using various host cell systems. One of the most effective systems is the methylotrophic yeast, Pichia pastoris . This yeast has emerged as a preferred host due to its shorter and less immunogenic glycosylation pattern, higher cell density growth, and higher secreted protein yield compared to other systems like Saccharomyces cerevisiae .
Advantages of Pichia pastoris
- Higher Yield: Pichia pastoris can achieve higher cell density growth and higher secreted protein yield than Saccharomyces cerevisiae .
- Glycosylation Pattern: The glycosylation pattern in Pichia pastoris is shorter and less immunogenic, making it more suitable for therapeutic applications .
- Purity and Potency: Purified rhGM-CSF from Pichia pastoris has been shown to be significantly more potent in terms of proliferative stimulating capacity on GM-CSF-dependent cell lines .
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